BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17647

Title: Backbone 13C, 15N, 1H chemical shift assignment of a thermostable mutant "6B" of a Lipase from Bacillus Subtilis   PubMed: 21925508

Deposition date: 2011-05-13 Original release date: 2011-10-12

Authors: Kamal, Md. Zahid; Ahmad, Shoeb; Trivikram Rao, Molugu; Vijayalakshmi, Amash; Sankaranarayanan, Rajan

Citation: Kamal, Md Zahid; Ahmad, Shoeb; Molugu, Trivikram Rao; Vijayalakshmi, Amash; Deshmukh, Mandar; Sankaranarayanan, Rajan; Rao, Nalam Madhusudhana. "In vitro evolved non-aggregating and thermostable lipase: structural and thermodynamic investigation."  J. Mol. Biol. 413, 726-741 (2011).

Assembly members:
6B, polymer, 181 residues, Formula weight is not available

Natural source:   Common Name: Bacillus subtilis   Taxonomy ID: 1423   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus subtilis

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
6B: AEHNPVVMVHGIGGSSSNFE GIKSYLVSQGWSRDKLYAVD FWDKTGTNYNNGPVLSRFVQ KVLDETGAKKVDIVAHSMGG ANTLYYIKYLDGGNKVANVV TLGGANRLTTDKAPPGTDPN QKILYTSIYSSDDEIVPNYL SRLDGARNVQIHGVGHMGLL YSPQVYSLIKEGLNGGGQNT N

Data sets:
Data typeCount
13C chemical shifts427
15N chemical shifts151
1H chemical shifts151

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
16B1

Entities:

Entity 1, 6B 181 residues - Formula weight is not available

1   ALAGLUHISASNPROVALVALMETVALHIS
2   GLYILEGLYGLYSERSERSERASNPHEGLU
3   GLYILELYSSERTYRLEUVALSERGLNGLY
4   TRPSERARGASPLYSLEUTYRALAVALASP
5   PHETRPASPLYSTHRGLYTHRASNTYRASN
6   ASNGLYPROVALLEUSERARGPHEVALGLN
7   LYSVALLEUASPGLUTHRGLYALALYSLYS
8   VALASPILEVALALAHISSERMETGLYGLY
9   ALAASNTHRLEUTYRTYRILELYSTYRLEU
10   ASPGLYGLYASNLYSVALALAASNVALVAL
11   THRLEUGLYGLYALAASNARGLEUTHRTHR
12   ASPLYSALAPROPROGLYTHRASPPROASN
13   GLNLYSILELEUTYRTHRSERILETYRSER
14   SERASPASPGLUILEVALPROASNTYRLEU
15   SERARGLEUASPGLYALAARGASNVALGLN
16   ILEHISGLYVALGLYHISMETGLYLEULEU
17   TYRSERPROGLNVALTYRSERLEUILELYS
18   GLUGLYLEUASNGLYGLYGLYGLNASNTHR
19   ASN

Samples:

sample_1: 6B, [U-13C; U-15N; 2H (80%)], 0.5 mM; 6B, [15N], 0.2 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.05 M; pH: 5.7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D HN(CA)CBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin, Keller and Wuthrich - chemical shift assignment, collection

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts